AU2008303796B2 - Heparin-binding epidermal growth factor-like growth factor antigen binding proteins - Google Patents
Heparin-binding epidermal growth factor-like growth factor antigen binding proteins Download PDFInfo
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- AU2008303796B2 AU2008303796B2 AU2008303796A AU2008303796A AU2008303796B2 AU 2008303796 B2 AU2008303796 B2 AU 2008303796B2 AU 2008303796 A AU2008303796 A AU 2008303796A AU 2008303796 A AU2008303796 A AU 2008303796A AU 2008303796 B2 AU2008303796 B2 AU 2008303796B2
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Priority Applications (1)
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| AU2013204186A AU2013204186A1 (en) | 2007-09-26 | 2013-04-08 | Heparin-binding epidermal growth factor-like growth factor antigen binding proteins |
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| PCT/EP2008/008233 WO2009040134A1 (en) | 2007-09-26 | 2008-09-26 | Heparin-binding epidermal growth factor-like growth factor antigen binding proteins |
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| AU2013204186A Division AU2013204186A1 (en) | 2007-09-26 | 2013-04-08 | Heparin-binding epidermal growth factor-like growth factor antigen binding proteins |
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| US8975374B2 (en) | 2006-10-20 | 2015-03-10 | Chugai Seiyaku Kabushiki Kaisha | Pharmaceutical composition comprising anti-HB-EGF antibody as active ingredient |
| EP2093237B1 (en) * | 2006-10-20 | 2015-12-30 | Chugai Seiyaku Kabushiki Kaisha | Anti-cancer agent comprising anti-hb-egf antibody as active ingredient |
| EP2078731A4 (en) * | 2006-10-20 | 2012-08-01 | Forerunner Pharma Res Co Ltd | PHARMACEUTICAL COMPOSITION COMPRISING ANTI-HB-EGF ANTIBODY AS ACTIVE INGREDIENT |
| IL199534A (en) | 2007-01-05 | 2013-01-31 | Univ Zuerich | An isolated human antibody capable of detecting a neoepitope in a disease-related protein, a polynucleotide encoding an antibody, a vector containing the polynucleotide, a host cell containing the polynucleotide or vector, a preparation containing the antibody and related methods and uses. |
| CA2709354C (en) * | 2007-12-21 | 2014-06-17 | Amgen Inc. | Anti-amyloid antibodies and uses thereof |
| GB0807018D0 (en) * | 2008-04-17 | 2008-05-21 | Fusion Antibodies Ltd | Antibodies and treatment |
| PT2370466E (pt) | 2008-12-19 | 2015-09-21 | Univ Zuerich | Autoanticorpos humanos anti-alfa-sinucleína |
| US8399625B1 (en) * | 2009-06-25 | 2013-03-19 | ESBATech, an Alcon Biomedical Research Unit, LLC | Acceptor framework for CDR grafting |
| US20120282173A1 (en) * | 2009-08-17 | 2012-11-08 | Forerunner Pharma Research Co., Ltd. | Pharmaceutical composition comprising anti-hb-egf antibody as active ingredient |
| JP5806935B2 (ja) * | 2009-08-17 | 2015-11-10 | 中外製薬株式会社 | 抗ｈｂ−ｅｇｆ抗体を有効成分として含む医薬組成物 |
| UA109888C2 (uk) | 2009-12-07 | 2015-10-26 | ІЗОЛЬОВАНЕ АНТИТІЛО АБО ЙОГО ФРАГМЕНТ, ЩО ЗВ'ЯЗУЄТЬСЯ З β-КЛОТО, РЕЦЕПТОРАМИ FGF І ЇХНІМИ КОМПЛЕКСАМИ | |
| WO2011119948A1 (en) * | 2010-03-26 | 2011-09-29 | Kolltan Pharmaceuticals, Inc. | Anti-kit antibodies and uses thereof |
| CN103796679B (zh) | 2011-06-23 | 2016-10-19 | 比奥根国际神经科学公司 | 抗-α突触核蛋白结合分子 |
| EP2817335A1 (en) * | 2012-02-22 | 2014-12-31 | U3 Pharma GmbH | Combination of hb-egf binding protein and egfr inhibitor |
| FR2988393B1 (fr) | 2012-03-20 | 2014-05-09 | Commissariat Energie Atomique | Inhibiteur de l'hb-egf derive du domaine r de la toxine diphterique pour le traitement des maladies associees a l'activation de la voie hb-egf/egfr |
| BR112015022260B1 (pt) | 2013-03-13 | 2023-05-16 | Prothena Biosciences Limited | Anticorpo monoclonal que se liga ao tau, polinucleotídeo, composição farmacêutica e uso de um anticorpo |
| US9840560B2 (en) * | 2013-03-15 | 2017-12-12 | Alper Biotech Llc | Monoclonal antibodies to EGFR, and uses therefor |
| WO2014174596A1 (ja) * | 2013-04-23 | 2014-10-30 | 株式会社医学生物学研究所 | ヘパリン結合上皮増殖因子様増殖因子に対する機能性モノクローナル抗体 |
| JP5838427B2 (ja) * | 2013-04-23 | 2016-01-06 | 株式会社医学生物学研究所 | ヘパリン結合上皮増殖因子様増殖因子に対する機能性モノクローナル抗体 |
| MA41115A (fr) | 2014-12-02 | 2017-10-10 | Biogen Int Neuroscience Gmbh | Procédé de traitement de la maladie d'alzheimer |
| SG10201913276WA (en) * | 2015-09-01 | 2020-02-27 | Agenus Inc | Anti-pd-1 antibodies and methods of use thereof |
| GEP20207174B (en) | 2015-11-18 | 2020-11-10 | Merck Sharp & Dohme | Ctla4 binders |
| MX2018008939A (es) | 2016-01-22 | 2019-08-21 | Merck Sharp & Dohme | Anticuerpos anti-factor de la coagulacion xi. |
| CA3022765A1 (en) | 2016-05-02 | 2017-11-09 | Prothena Biosciences Limited | Antibodies recognizing tau |
| ES2933491T3 (es) | 2016-05-02 | 2023-02-09 | Prothena Biosciences Ltd | Inmunoterapia tau |
| IL262726B2 (en) | 2016-05-02 | 2024-07-01 | Prothena Biosciences Ltd | Antibodies that recognize tau |
| AR108717A1 (es) | 2016-06-14 | 2018-09-19 | Merck Sharp & Dohme | Anticuerpos antifactor de la coagulación xi |
| CN118634323A (zh) | 2016-12-07 | 2024-09-13 | 艾吉纳斯公司 | 抗体和其使用方法 |
| SG11201910066QA (en) | 2017-05-02 | 2019-11-28 | Prothena Biosciences Ltd | Antibodies recognizing tau |
| IL272773B2 (en) | 2017-08-22 | 2024-06-01 | Biogen Ma Inc | Pharmaceutical preparations containing anti-amyloid cell antibodies |
| US11525002B2 (en) | 2017-10-11 | 2022-12-13 | Board Of Regents, The University Of Texas System | Human PD-L1 antibodies and methods of use therefor |
| JP7390294B2 (ja) * | 2018-01-08 | 2023-12-01 | スサヴィオン バイオサイエンシーズ インコーポレイテッド | 糖鎖模倣ペプチドを用いて癌を処置する組成物および方法 |
| EP3768298A4 (en) * | 2018-03-23 | 2021-12-08 | Board of Regents, The University of Texas System | HUMAN ANTI-PD-L2 ANTIBODIES AND PROCESSES FOR USE |
| CN109535252B (zh) * | 2018-12-17 | 2020-04-21 | 江苏莱森生物科技研究院有限公司 | 一种抗hb-egf单克隆抗体及其制备方法 |
| CN109580959B (zh) * | 2018-12-17 | 2020-03-31 | 江苏莱森生物科技研究院有限公司 | 一种检测肝素结合性表皮生长因子的elisa试剂盒 |
| AU2020231366A1 (en) | 2019-03-03 | 2021-08-12 | Prothena Biosciences Limited | Antibodies recognizing tau |
| US11299545B2 (en) * | 2019-04-04 | 2022-04-12 | Janssen Biotech, Inc. | Anti-HLA-C antibodies and uses thereof |
| CA3201588A1 (en) * | 2020-12-09 | 2022-06-16 | David Campbell | Compositions and methods related to tumor activated antibodies targeting psma and effector cell antigens |
| WO2022150660A1 (en) * | 2021-01-08 | 2022-07-14 | 10X Genomics, Inc. | Antigen-binding polypeptides specific for coronaviruses and uses thereof |
| AU2023216372A1 (en) * | 2022-02-07 | 2024-09-26 | Cornell University | Targeting art1 for cancer immunotherapy |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007142277A1 (ja) * | 2006-06-06 | 2007-12-13 | Kyowa Hakko Kirin Co., Ltd. | ヘパリン結合上皮細胞増殖因子様増殖因子に結合するモノクローナル抗体 |
| WO2008047925A1 (fr) * | 2006-10-20 | 2008-04-24 | Forerunner Pharma Research Co., Ltd. | Composition pharmaceutique comprenant un anticorps anti-hb-egf comme ingrédient actif |
| WO2008047914A1 (fr) * | 2006-10-20 | 2008-04-24 | Forerunner Pharma Research Co., Ltd. | Agent anticancéreux comprenant un anticorps anti-hb-egf en tant qu'ingrédient actif |
Family Cites Families (65)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3180193A (en) | 1963-02-25 | 1965-04-27 | Benedict David | Machines for cutting lengths of strip material |
| GB1047304A (pt) * | 1963-07-05 | |||
| US3773919A (en) * | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| US4263428A (en) | 1978-03-24 | 1981-04-21 | The Regents Of The University Of California | Bis-anthracycline nucleic acid function inhibitors and improved method for administering the same |
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| ATE12348T1 (de) | 1980-11-10 | 1985-04-15 | Gersonde Klaus Prof Dr | Verfahren zur herstellung von lipid-vesikeln durch ultraschallbehandlung, anwendung des verfahrens und vorrichtung zur durchfuehrung des verfahrens. |
| IE52535B1 (en) | 1981-02-16 | 1987-12-09 | Ici Plc | Continuous release pharmaceutical compositions |
| US4485045A (en) * | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
| JPS58118008A (ja) | 1982-01-06 | 1983-07-13 | Nec Corp | デ−タ処理装置 |
| DE3374837D1 (en) | 1982-02-17 | 1988-01-21 | Ciba Geigy Ag | Lipids in the aqueous phase |
| JPS58166634A (ja) | 1982-03-29 | 1983-10-01 | Toshiba Corp | 有機溶媒電池用正極 |
| JPS58166633A (ja) | 1982-03-29 | 1983-10-01 | Toshiba Corp | 有機溶媒電池用正極 |
| DE3218121A1 (de) | 1982-05-14 | 1983-11-17 | Leskovar, Peter, Dr.-Ing., 8000 München | Arzneimittel zur tumorbehandlung |
| EP0102324A3 (de) | 1982-07-29 | 1984-11-07 | Ciba-Geigy Ag | Lipide und Tenside in wässriger Phase |
| US4544545A (en) | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
| HUT35524A (en) | 1983-08-02 | 1985-07-29 | Hoechst Ag | Process for preparing pharmaceutical compositions containing regulatory /regulative/ peptides providing for the retarded release of the active substance |
| EP0142641B1 (de) | 1983-09-26 | 1991-01-16 | Udo Dr. Ehrenfeld | Mittel und Erzeugnis für die Diagnose und Therapie von Tumoren sowie zur Behandlung von Schwächen der zelligen und humoralen Immunabwehr |
| EP0143949B1 (en) | 1983-11-01 | 1988-10-12 | TERUMO KABUSHIKI KAISHA trading as TERUMO CORPORATION | Pharmaceutical composition containing urokinase |
| US4740461A (en) * | 1983-12-27 | 1988-04-26 | Genetics Institute, Inc. | Vectors and methods for transformation of eucaryotic cells |
| JPS62170639A (ja) | 1986-01-22 | 1987-07-27 | 株式会社システムメンテナンス | 防蟻板の取付け工法 |
| US4959455A (en) * | 1986-07-14 | 1990-09-25 | Genetics Institute, Inc. | Primate hematopoietic growth factors IL-3 and pharmaceutical compositions |
| US4912040A (en) | 1986-11-14 | 1990-03-27 | Genetics Institute, Inc. | Eucaryotic expression system |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
| WO1991010741A1 (en) * | 1990-01-12 | 1991-07-25 | Cell Genesys, Inc. | Generation of xenogeneic antibodies |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6673986B1 (en) * | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
| FR2664073A1 (fr) | 1990-06-29 | 1992-01-03 | Thomson Csf | Moyens de marquage d'objets, procede de realisation et dispositif de lecture. |
| CA2089661C (en) | 1990-08-29 | 2007-04-03 | Nils Lonberg | Transgenic non-human animals capable of producing heterologous antibodies |
| US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US6300129B1 (en) | 1990-08-29 | 2001-10-09 | Genpharm International | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5814318A (en) * | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5612205A (en) | 1990-08-29 | 1997-03-18 | Genpharm International, Incorporated | Homologous recombination in mammalian cells |
| US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5789650A (en) * | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) * | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625126A (en) * | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| WO1992022670A1 (en) | 1991-06-12 | 1992-12-23 | Genpharm International, Inc. | Early detection of transgenic embryos |
| AU2235992A (en) | 1991-06-14 | 1993-01-12 | Genpharm International, Inc. | Transgenic immunodeficient non-human animals |
| AU2515992A (en) | 1991-08-20 | 1993-03-16 | Genpharm International, Inc. | Gene targeting in animal cells using isogenic dna constructs |
| CA2124967C (en) | 1991-12-17 | 2008-04-08 | Nils Lonberg | Transgenic non-human animals capable of producing heterologous antibodies |
| AU4541093A (en) | 1992-06-18 | 1994-01-24 | Genpharm International, Inc. | Methods for producing transgenic non-human animals harboring a yeast artificial chromosome |
| ES2301158T3 (es) | 1992-07-24 | 2008-06-16 | Amgen Fremont Inc. | Produccion de anticuerpos xenogenicos. |
| US5981175A (en) | 1993-01-07 | 1999-11-09 | Genpharm Internation, Inc. | Methods for producing recombinant mammalian cells harboring a yeast artificial chromosome |
| AU6819494A (en) | 1993-04-26 | 1994-11-21 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625825A (en) | 1993-10-21 | 1997-04-29 | Lsi Logic Corporation | Random number generating apparatus for an interface unit of a carrier sense with multiple access and collision detect (CSMA/CD) ethernet data network |
| US5643763A (en) | 1994-11-04 | 1997-07-01 | Genpharm International, Inc. | Method for making recombinant yeast artificial chromosomes by minimizing diploid doubling during mating |
| AU2466895A (en) | 1995-04-28 | 1996-11-18 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| ATE352613T1 (de) | 1995-08-29 | 2007-02-15 | Kirin Brewery | Chimäres tier und methode zu dessen herstellung |
| PT1500329E (pt) | 1996-12-03 | 2012-06-18 | Amgen Fremont Inc | Anticorpos humanos que se ligam especificamente ao tnf alfa humano |
| US6833268B1 (en) | 1999-06-10 | 2004-12-21 | Abgenix, Inc. | Transgenic animals for producing specific isotypes of human antibodies via non-cognate switch regions |
| DE19932688B4 (de) | 1999-07-13 | 2009-10-08 | Scil Proteins Gmbh | Design von Beta-Faltblatt-Proteinen des gamma-II-kristallins antikörperähnlichen |
| FR2828104B1 (fr) * | 2001-08-01 | 2005-06-24 | Chu Montpellier | Utilisation d'inhibiteurs du facteur de croissance epidermique liant l'heparine ou d'inhibiteurs de ses recepteurs pour la preparation de medicaments utiles pour traiter le myelome |
| GB0201284D0 (en) * | 2002-01-21 | 2002-03-06 | Isis Innovation | Screening methods for contraceptive and fertility agents |
| KR101531400B1 (ko) * | 2003-06-27 | 2015-06-26 | 암젠 프레몬트 인코포레이티드 | 상피 성장 인자 수용체의 결실 돌연변이체 지향 항체 및 그용도 |
| US7833731B2 (en) * | 2004-03-31 | 2010-11-16 | Canon Kabushiki Kaisha | Gold-binding protein and use thereof |
| US20050227289A1 (en) * | 2004-04-09 | 2005-10-13 | Reilly Edward B | Antibodies to erythropoietin receptor and uses thereof |
| SI1838733T1 (sl) * | 2004-12-21 | 2011-12-30 | Medimmune Ltd | Protitelesa usmerjena na angiopoietin-2 in njih uporaba |
| JP6071725B2 (ja) | 2013-04-23 | 2017-02-01 | カルソニックカンセイ株式会社 | 電気自動車の駆動力制御装置 |
| US11284893B2 (en) | 2019-04-02 | 2022-03-29 | Covidien Lp | Stapling device with articulating tool assembly |
-
2008
- 2008-09-26 SG SG2013003140A patent/SG187477A1/en unknown
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- 2014-07-28 US US14/444,912 patent/US20160009796A9/en not_active Abandoned
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007142277A1 (ja) * | 2006-06-06 | 2007-12-13 | Kyowa Hakko Kirin Co., Ltd. | ヘパリン結合上皮細胞増殖因子様増殖因子に結合するモノクローナル抗体 |
| WO2008047925A1 (fr) * | 2006-10-20 | 2008-04-24 | Forerunner Pharma Research Co., Ltd. | Composition pharmaceutique comprenant un anticorps anti-hb-egf comme ingrédient actif |
| WO2008047914A1 (fr) * | 2006-10-20 | 2008-04-24 | Forerunner Pharma Research Co., Ltd. | Agent anticancéreux comprenant un anticorps anti-hb-egf en tant qu'ingrédient actif |
Non-Patent Citations (2)
| Title |
|---|
| Itoh, Y. et al. 2005 Cytokine, vol. 29, pp. 275-282 * |
| Mishima, K. et al. 1998 Acta Neuropathologica, vol. 96, pp. 322-328 * |
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